The iron and cobalt pigments : biosynthesis, structure, and degradation /

Detalles Bibliográficos
Clasificación:Libro Electrónico
Otros Autores: Kadish, Karl M., Smith, Kevin M., Guilard, Roger
Formato: Electrónico eBook
Idioma:Inglés
Publicado: San Diego, Calif. : Academic Press, 2003.
Colección:The porphyrin handbook ; v. 12
Temas:
Pigments.
Porphyrins.
Organocobalt compounds.
Organoiron compounds.
Porphyrines.
Compos�es d'organocobalt.
Compos�es organoferreux.
pigment.
SCIENCE > Chemistry > Organic.
Acceso en línea:Texto completo
Tabla de Contenidos:
  • Front Cover; The Porphyrin Handbook: The Iron and Cobalt Pigments: Biosynthesis, Structure, and Degradation; Copyright Page; Table of Contents; Preface; Contributors to Volumes 120; Contents of Volumes 1-20; Chapter 69. Regulatory Mechanisms of Eukaryotic Tetrapyrrole Biosynthesis; I. Introduction; II. Differences and Similarities of the Metabolic Pathway in Animals and Plants; III. Control of Mammalian Heme Synthesis; IV. Control of Plant Tetrapyrrole Biosynthesis; V. The Regulatory Network; VI. Conclusion; References; Chapter 70. The Biosynthesis of Coproporphyrinogen III; I. Introduction.
  • II. The Biosynthesis of 5-Aminolaevulinic AcidIII. The Transformation of 5-Aminolaevulinic Acid into Uroporphyrinogen III; IV. The Transformation of Uroporphyrinogen III into Coproporphyrinogen III; V. Further Conversion of Coproporphyrinogen III into Haem and Alternative Pathways that Transform Uroporphyrinogen III into Precorrin-2, Sirohaem, Factor F4 30 and Vitamin B12; References; Chapter 71. Coproporphyrinogen III and Protoporphyrinogen IX Oxidases; I. Coproporphyrinogen III Oxidase; II. Protoporphyrinogen IX Oxidase; References; Chapter 72. Ferrochelatase; I. Background.
  • II. Studies on Enzyme ActivityIII. Enzyme Mechanism; IV. Crystal Structures of Ferrochelatases; V. Proposed Enzyme Mechanism; VI. Plant Ferrochelatases; VII. Nonferrochelatase-Catalyzed Metalation; VIII. Mammalian Genomic Organization and Regulation; IX. Erythropoietic Protoporphyria; X. Ferrochelatase and Iron Metabolism; XI. Diversity and Ferrochelatase Evolution; References; Chapter 73. The Family of d-Type Hemes: Tetrapyrroles with Unusual Substituents; I. Introduction; II. Heme d1; III. Hemes d; IV. Honorary d-type Hemes; V. Concluding Remarks; References.
  • Chapter 74. Biosynthesis and Role of Heme O and Heme AI. Variations in Hemes and Related Compounds; II. Biosynthesis of Heme O; III. Biosynthesis of Heme A; IV. Role of Farnesylated Hemes; V. Organization of Genes Coding the Heme-Copper Terminal Oxidases and Heme O and Heme A Synthases; References; Chapter 75. Heme Oxygenase Structure and Mechanism; I. Introduction; II. Biological Functions of Heme Oxygenase; III. Heme Oxygenase Proteins; IV. Heme Oxygenase Structure; V. Interaction with Cytochrome P450 Reductase and Reductive Reactions; VI. Small Physiological Ligands.
  • VII. Substrate SpecificityVIII. Heme Oxygenase Model Systems; IX. Stage One: [alpha]-meso-Hydroxylation; X. Stage Two: [alpha]-meso-Hydroxyheme to Verdoheme; XI. Stage Three: Verdoheme to Biliverdin; XII. Heme Oxygenase Kinetics; XIII. Implications of Electrophilic Heme Oxidation by an Felll-OOH Intermediate; References; Chapter 76. Genetic and Mechanistic Exploration of the Two Pathways of Vitamin B12 Biosynthesis; I. Introduction; II. Genetics of Cobalamin Biosynthesis; III. Comparison of the Aerobic and Anaerobic Pathways to Cobalamin from Aminolevulinic Acid.
  • IV. Genomics of Cobalamin Biosynthesis
  • Are there Other Variations in the Route to B12?

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